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Q27452

- PRP2_BOMMO

UniProt

Q27452 - PRP2_BOMMO

Protein

Phenoloxidase subunit 2

Gene
N/A
Organism
Bombyx mori (Silk moth)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 2 (01 Jan 1999)
      Previous versions | rss
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    Functioni

    This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the rate-limiting conversions of tyrosine to DOPA, DOPA to DOPA-quinone and possibly 5,6 dihydroxyindole to indole-5'6 quinone.

    Catalytic activityi

    2 L-dopa + O2 = 2 dopaquinone + 2 H2O.
    L-tyrosine + O2 = dopaquinone + H2O.

    Cofactori

    Binds 2 copper ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi213 – 2131Copper ABy similarity
    Metal bindingi217 – 2171Copper ABy similarity
    Metal bindingi243 – 2431Copper ABy similarity
    Metal bindingi366 – 3661Copper BBy similarity
    Metal bindingi370 – 3701Copper BBy similarity
    Metal bindingi406 – 4061Copper BBy similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. monophenol monooxygenase activity Source: UniProtKB

    GO - Biological processi

    1. defense response Source: UniProtKB
    2. melanin biosynthetic process from tyrosine Source: UniProtKB

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Melanin biosynthesis

    Keywords - Ligandi

    Copper, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phenoloxidase subunit 2 (EC:1.14.18.1)
    Alternative name(s):
    PO 2
    Tyrosinase 2
    OrganismiBombyx mori (Silk moth)Imported
    Taxonomic identifieri7091 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaBombycoideaBombycidaeBombycinaeBombyx
    ProteomesiUP000005204: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 51511 PublicationPRO_0000035901Add
    BLAST
    Chaini52 – 693642Phenoloxidase subunit 2PRO_0000035902Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi26 – 261N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi64 – 641N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi462 – 4621N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi494 – 4941N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi583 ↔ 627By similarity
    Disulfide bondi585 ↔ 634By similarity
    Glycosylationi680 – 6801N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    The N-terminus is blocked.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Expressioni

    Tissue specificityi

    Synthesized by hemocytes and released into the hemolymph plasma.1 Publication

    Interactioni

    Subunit structurei

    Heterodimer.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliQ27452.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the tyrosinase family.Curated

    Phylogenomic databases

    OMAiIDEMERW.
    OrthoDBiEOG7XPZ54.

    Family and domain databases

    Gene3Di1.10.1280.10. 1 hit.
    1.20.1370.10. 1 hit.
    2.60.40.1520. 1 hit.
    InterProiIPR013788. Hemocyanin/hexamerin.
    IPR000896. Hemocyanin/hexamerin_mid_dom.
    IPR005203. Hemocyanin_C.
    IPR005204. Hemocyanin_N.
    IPR014756. Ig_E-set.
    IPR002227. Tyrosinase_Cu-bd.
    IPR008922. Unchr_di-copper_centre.
    [Graphical view]
    PANTHERiPTHR11511. PTHR11511. 1 hit.
    PfamiPF03723. Hemocyanin_C. 1 hit.
    PF00372. Hemocyanin_M. 1 hit.
    PF03722. Hemocyanin_N. 1 hit.
    [Graphical view]
    PRINTSiPR00187. HAEMOCYANIN.
    SUPFAMiSSF48050. SSF48050. 1 hit.
    SSF48056. SSF48056. 1 hit.
    SSF81296. SSF81296. 1 hit.
    PROSITEiPS00209. HEMOCYANIN_1. 1 hit.
    PS00210. HEMOCYANIN_2. 1 hit.
    PS00498. TYROSINASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q27452-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADVFESLEL LFDRPNEPLI TPKGENNSVF QLTEQFLTED YANNGIELNN    50
    RFGDDASEKI PLKNLSKLPE FKIATQLPKD AEFSLFLPKH QEMANELLGV 100
    LMDVPENELQ DLLSTCAFAR VNLNPQLFNY CYSVALMHRR DTRKVRVKNF 150
    AEVFPSKFLD SQVFTQARET AAVIPPDVPR IPIIIPRDYT ATDLEEEHRL 200
    AYWREDIGIN LHHYHWHLVY PFTANDLSIV AKDRRGELFF YMHQQVIARF 250
    NCERLCNSLK RVKKFSNWRE PIPEAYFPKL DSLTSSRGWP PRQSGMQWQD 300
    LNRAAEGLFV TIDEMERWRR NVEEAIATGT VRLPNGQTRP LDIDTLGNML 350
    ESSALSPNRE LYGSIHNNGH SFTAYMHDPE HRYLEQFGVI ADEATTMRDP 400
    FFYRWHAYID DVFQKHKESA YVRPYTRSEL ENPGVQVRSV SVETPGGQPN 450
    TLNTFWMLSD VNLSRGLDFS DNGPVYARFT HLNYRHFSYR INVNNTGSSR 500
    RTTVRIFITP KFDERNVPWI FSDQRKMCIE MDRFVTVLNA GENNIVRQST 550
    ESSITIPFEQ TFRDLSAQGN DPRRDELATF NYCGCGWPQH MLVPKGTEAG 600
    MPFQLFVMLS NYDLDRIDQD DGKQLTCVEA SSFCGLKDKK YPDRRAMGFP 650
    FDRPSSSATS LQDFILPNMG LQDITIQLQN VTEPNPRNPP MSV 693
    Length:693
    Mass (Da):80,119
    Last modified:January 1, 1999 - v2
    Checksum:i013114DF4CC1A926
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti433 – 4331P → Q AA sequence (PubMed:7644494)Curated

    Mass spectrometryi

    Molecular mass is 81105 Da from positions 52 - 693. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D49371 mRNA. Translation: BAA08369.1.
    AB048762 mRNA. Translation: BAB41101.1.
    RefSeqiNP_001037534.1. NM_001044069.1.
    UniGeneiBmo.1389.

    Genome annotation databases

    EnsemblMetazoaiBGIBMGA013115-RA; BGIBMGA013115-TA; BGIBMGA013115.
    GeneIDi693073.
    KEGGibmor:693073.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D49371 mRNA. Translation: BAA08369.1 .
    AB048762 mRNA. Translation: BAB41101.1 .
    RefSeqi NP_001037534.1. NM_001044069.1.
    UniGenei Bmo.1389.

    3D structure databases

    ProteinModelPortali Q27452.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai BGIBMGA013115-RA ; BGIBMGA013115-TA ; BGIBMGA013115 .
    GeneIDi 693073.
    KEGGi bmor:693073.

    Organism-specific databases

    CTDi 693073.

    Phylogenomic databases

    OMAi IDEMERW.
    OrthoDBi EOG7XPZ54.

    Family and domain databases

    Gene3Di 1.10.1280.10. 1 hit.
    1.20.1370.10. 1 hit.
    2.60.40.1520. 1 hit.
    InterProi IPR013788. Hemocyanin/hexamerin.
    IPR000896. Hemocyanin/hexamerin_mid_dom.
    IPR005203. Hemocyanin_C.
    IPR005204. Hemocyanin_N.
    IPR014756. Ig_E-set.
    IPR002227. Tyrosinase_Cu-bd.
    IPR008922. Unchr_di-copper_centre.
    [Graphical view ]
    PANTHERi PTHR11511. PTHR11511. 1 hit.
    Pfami PF03723. Hemocyanin_C. 1 hit.
    PF00372. Hemocyanin_M. 1 hit.
    PF03722. Hemocyanin_N. 1 hit.
    [Graphical view ]
    PRINTSi PR00187. HAEMOCYANIN.
    SUPFAMi SSF48050. SSF48050. 1 hit.
    SSF48056. SSF48056. 1 hit.
    SSF81296. SSF81296. 1 hit.
    PROSITEi PS00209. HEMOCYANIN_1. 1 hit.
    PS00210. HEMOCYANIN_2. 1 hit.
    PS00498. TYROSINASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of insect pro-phenol oxidase: a copper-containing protein homologous to arthropod hemocyanin."
      Kawabata T., Yasuhara Y., Ochiai M., Matsuura S., Ashida M.
      Proc. Natl. Acad. Sci. U.S.A. 92:7774-7778(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Strain: Kinshu X Showa1 Publication.
      Tissue: Hemocyte1 Publication.
    2. Asano T., Ashida M.
      Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Reexamination of properties of phenoloxidase isolated from larval hemolymph of the silkworm Bombyx mori."
      Yasuhara Y., Koizumi Y., Katagiri C., Ashida M.
      Arch. Biochem. Biophys. 320:14-23(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: MASS SPECTROMETRY.
      Tissue: Hemocyte1 Publication.

    Entry informationi

    Entry nameiPRP2_BOMMO
    AccessioniPrimary (citable) accession number: Q27452
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: January 1, 1999
    Last modified: October 1, 2014
    This is version 81 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3